Q94A52 · RH2_ARATH

Function

function

ATP-dependent RNA helicase. Core component of the splicing-dependent multiprotein exon junction complex (EJC) deposited at splice junctions on mRNAs. The EJC is a dynamic structure consisting of core proteins and several peripheral nuclear and cytoplasmic associated factors that join the complex only transiently either during EJC assembly or during subsequent mRNA metabolism. The EJC marks the position of the exon-exon junction in the mature mRNA for the gene expression machinery and the core components remain bound to spliced mRNAs throughout all stages of mRNA metabolism thereby influencing downstream processes including nuclear mRNA export, subcellular mRNA localization, translation efficiency and nonsense-mediated mRNA decay (NMD). Its RNA-dependent ATPase and RNA-helicase activities are induced by MLN51/CASC3, but abolished in presence of the MAGO-Y14 heterodimer, thereby trapping the ATP-bound EJC core onto spliced mRNA in a stable conformation. The inhibition of ATPase activity by the MAGO-Y14 heterodimer increases the RNA-binding affinity of the EJC (By similarity).
Plays a role in abiotic stress adaptation. Can regulate abiotic stress resistance partially via the control of acetoacetyl-CoA thiolase 2 (AC Q8S4Y1) expression (PubMed:26883227).
(Microbial infection) Functions as a host RNA helicase that is co-opted by the tombusvirus (TBSV) RNA replication enhancer to greatly enhance tombusvirus replication. Interacts with the viral minus-strand RNA and the replication proteins within the viral replicase.

Catalytic activity

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site79-86ATP (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytosol
Cellular Componentexon-exon junction complex
Cellular Componentnuclear speck
Cellular Componentnucleolus
Cellular Componentnucleoplasm
Cellular Componentnucleus
Molecular FunctionATP binding
Molecular FunctionATP hydrolysis activity
Molecular FunctionmRNA binding
Molecular FunctionRNA helicase activity
Biological ProcessmRNA processing
Biological ProcessmRNA transport
Biological Processnuclear-transcribed mRNA catabolic process, nonsense-mediated decay
Biological Processregulation of translation
Biological Processresponse to hypoxia
Biological ProcessRNA splicing

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Eukaryotic initiation factor 4A-III homolog
  • EC number
  • Short names
    AteIF4AIII
    ; eIF-4A-III
    ; eIF4A-III
  • Alternative names
    • DEAD-box ATP-dependent RNA helicase 2
      (AtRH02
      )

Gene names

    • Name
      EIF4A3
    • Synonyms
      RH2
    • ORF names
      MMB12.25
      , MMB12.4
    • Ordered locus names
      At3g19760

Organism names

  • Taxonomic identifier
  • Strain
    • cv. Columbia
  • Taxonomic lineage
    Eukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > malvids > Brassicales > Brassicaceae > Camelineae > Arabidopsis

Accessions

  • Primary accession
    Q94A52
  • Secondary accessions
    • Q9ZS14

Proteomes

Organism-specific databases

Genome annotation databases

Subcellular Location

Nucleus, nucleoplasm
Nucleus, nucleolus
Nucleus speckle
Nucleus
Cytoplasm
Note: Hypoxia causes transition from diffuse nucleoplasmic localization to accumulation in speckles in nuclei of root cells (PubMed:19435936).
Localized to the nucleus when hypophosphorylated. Hyperphosphorylation of EIF4A3 increases its cytoplasmic localization (PubMed:26887918).
Nucleocytoplasmic shuttling protein. Travels to the cytoplasm as part of the exon junction complex (EJC) bound to mRNA (By similarity).

Keywords

Phenotypes & Variants

Disruption phenotype

No visible phenotype under normal growth conditions, but mutant seedlings show increased sensitivity to cold and heat stresses.

Features

Showing features for mutagenesis.

TypeIDPosition(s)Description
Mutagenesis100Increases cytoplasmic localization; when associated with D-101.
Mutagenesis101Increases cytoplasmic localization; when associated with D-100.

Variants

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The viewer provides 11 variants from UniProt as well as other sources including ClinVar and dbSNP.

Go to variant viewer

PTM/Processing

Features

Showing features for chain, modified residue.

TypeIDPosition(s)Description
ChainPRO_00002391441-408Eukaryotic initiation factor 4A-III homolog
Modified residue100Phosphoserine
Modified residue101Phosphoserine

Post-translational modification

Phosphorylated at Ser-100 and Ser-101. Phosphorylation status of Ser-100 and Ser-101 largely determines the subcellular localization of EIF4A3.

Keywords

Proteomic databases

PTM databases

Expression

Induction

Induced by cold and heat stresses.

Gene expression databases

Interaction

Subunit

Interacts with ALY4 (PubMed:19435936).
Interacts with MAGO (PubMed:26867216).
Interacts with CPL1/FRY2 (PubMed:26887918).

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for region, motif, domain.

TypeIDPosition(s)Description
Region1-20Disordered
Motif35-63Q motif
Domain66-236Helicase ATP-binding
Motif184-187DEAD box
Domain247-408Helicase C-terminal

Domain

The Q motif is unique to and characteristic of the DEAD box family of RNA helicases and controls ATP binding and hydrolysis.

Sequence similarities

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    408
  • Mass (Da)
    45,845
  • Last updated
    2006-05-30 v2
  • Checksum
    4BD11BBA58BAA0D9
MATANPGRGGGRRGGGAMDDDKLVFETTDGIEPITSFNDMGIKEDVLRGVYEYGFEKPSAIQQRAVMPILQGRDVIAQAQSGTGKTSMIALSVCQVVDTSSREVQALILSPTRELATQTEKTIQAIGLHANIQAHACIGGNSVGEDIRKLEHGVHVVSGTPGRVCDMIKRRSLRTRAIKLLILDESDEMLSRGFKDQIYDVYRYLPPDLQVCLVSATLPHEILEMTSKFMTEPVKILVKRDELTLEGIKQFFVAVEKEEWKFDTLCDLYDTLTITQAVIFCNTKRKVDYLSEKMRSHNFTVSSMHGDMPQKERDAIMNEFRSGDSRVLITTDVWARGIDVQQVSLVINYDLPNNRELYIHRIGRSGRFGRKGVAINFVKSDDIKILRDIEQYYSTQIDEMPMNVADLI

Sequence caution

The sequence BAB02563.1 differs from that shown. Reason: Erroneous initiation Truncated N-terminus.
The sequence CAA09195.1 differs from that shown. Reason: Frameshift

Features

Showing features for sequence conflict.

TypeIDPosition(s)Description
Sequence conflict114in Ref. 4; AAK91384/AAN72219

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AJ010456
EMBL· GenBank· DDBJ
CAA09195.1
EMBL· GenBank· DDBJ
mRNA Frameshift
AP000417
EMBL· GenBank· DDBJ
BAB02563.1
EMBL· GenBank· DDBJ
Genomic DNA Different initiation
CP002686
EMBL· GenBank· DDBJ
AEE76283.1
EMBL· GenBank· DDBJ
Genomic DNA
AY050367
EMBL· GenBank· DDBJ
AAK91384.1
EMBL· GenBank· DDBJ
mRNA
BT002207
EMBL· GenBank· DDBJ
AAN72219.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

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